Bovine heart cytochrome c was studied through cyclic voltammetry in mixed water-organic solvent solutions under different conditions of temperature and the thermodynamic properties DeltaS(rc)(o) and DeltaH(rc)(o) calculated by the dependence of Edegrees by temperature. The effect of the organic fraction of the solvent on the Edegrees values of the native cyt c was found to be determined mainly by the decrease in dielectric constant of the medium. Specific interactions on the protein surface do not seem to play a remarkable role. The thermodynamic properties changes induced by the organic fraction have been interpreted tentatively in terms of solvation properties of cytochrome c and structural features of the protein environment. (C) 2003 Elsevier Science B.V. All rights reserved.
Redox thermodynamics of cytochrome c in mixed water-organic solvent solutions / Borsari, Marco; Bellei, Marzia; Tavagnacco, C; Peressini, S; Millo, D; Costa, G.. - In: INORGANICA CHIMICA ACTA. - ISSN 0020-1693. - STAMPA. - 349:(2003), pp. 182-188. [10.1016/S0020-1693(03)00043-4]
Redox thermodynamics of cytochrome c in mixed water-organic solvent solutions
BORSARI, Marco;BELLEI, Marzia;
2003
Abstract
Bovine heart cytochrome c was studied through cyclic voltammetry in mixed water-organic solvent solutions under different conditions of temperature and the thermodynamic properties DeltaS(rc)(o) and DeltaH(rc)(o) calculated by the dependence of Edegrees by temperature. The effect of the organic fraction of the solvent on the Edegrees values of the native cyt c was found to be determined mainly by the decrease in dielectric constant of the medium. Specific interactions on the protein surface do not seem to play a remarkable role. The thermodynamic properties changes induced by the organic fraction have been interpreted tentatively in terms of solvation properties of cytochrome c and structural features of the protein environment. (C) 2003 Elsevier Science B.V. All rights reserved.
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